RZ1C_ARATH
ID RZ1C_ARATH Reviewed; 310 AA.
AC Q8RWN5;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 148.
DE RecName: Full=Glycine-rich RNA-binding protein RZ1C {ECO:0000305};
DE Short=AtRZ-1C {ECO:0000303|PubMed:20850334};
GN Name=RZ1C {ECO:0000305};
GN OrderedLocusNames=At5g04280 {ECO:0000312|Araport:AT5G04280};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-295, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY COLD, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=20850334; DOI=10.1016/j.plaphy.2010.08.013;
RA Kim W.Y., Kim J.Y., Jung H.J., Oh S.H., Han Y.S., Kang H.;
RT "Comparative analysis of Arabidopsis zinc finger-containing glycine-rich
RT RNA-binding proteins during cold adaptation.";
RL Plant Physiol. Biochem. 48:866-872(2010).
CC -!- FUNCTION: Binds RNA and DNA sequences non-specifically. May be involved
CC in tolerance to cold stress. {ECO:0000269|PubMed:20850334}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20850334}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, rosette and cauline leaves,
CC stems, floral buds and flowers. {ECO:0000269|PubMed:20850334}.
CC -!- INDUCTION: By cold stress. {ECO:0000269|PubMed:20850334}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:20850334}.
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DR EMBL; AL391716; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED90723.1; -; Genomic_DNA.
DR EMBL; AY092975; AAM12974.1; -; mRNA.
DR EMBL; AY114645; AAM47964.1; -; mRNA.
DR RefSeq; NP_196048.1; NM_120510.4.
DR AlphaFoldDB; Q8RWN5; -.
DR SMR; Q8RWN5; -.
DR BioGRID; 15587; 10.
DR IntAct; Q8RWN5; 7.
DR STRING; 3702.AT5G04280.1; -.
DR iPTMnet; Q8RWN5; -.
DR PaxDb; Q8RWN5; -.
DR PRIDE; Q8RWN5; -.
DR ProteomicsDB; 232877; -.
DR EnsemblPlants; AT5G04280.1; AT5G04280.1; AT5G04280.
DR GeneID; 830307; -.
DR Gramene; AT5G04280.1; AT5G04280.1; AT5G04280.
DR KEGG; ath:AT5G04280; -.
DR Araport; AT5G04280; -.
DR TAIR; locus:2179939; AT5G04280.
DR eggNOG; KOG0118; Eukaryota.
DR HOGENOM; CLU_012062_28_0_1; -.
DR InParanoid; Q8RWN5; -.
DR OMA; VGQDECF; -.
DR OrthoDB; 1579773at2759; -.
DR PhylomeDB; Q8RWN5; -.
DR PRO; PR:Q8RWN5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8RWN5; baseline and differential.
DR Genevisible; Q8RWN5; AT.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0003682; F:chromatin binding; IDA:TAIR.
DR GO; GO:0031490; F:chromatin DNA binding; IDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0003676; F:nucleic acid binding; IDA:TAIR.
DR GO; GO:0003723; F:RNA binding; IDA:TAIR.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IGI:TAIR.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IGI:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IEP:TAIR.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF00098; zf-CCHC; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding; Stress response; Zinc; Zinc-finger.
FT CHAIN 1..310
FT /note="Glycine-rich RNA-binding protein RZ1C"
FT /id="PRO_0000431282"
FT DOMAIN 7..85
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT ZN_FING 128..143
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 82..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862,
FT ECO:0007744|PubMed:19376835"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
SQ SEQUENCE 310 AA; 33486 MW; 219ED5F035432AE0 CRC64;
MAAKEGSRIF VGGLSPEVTD RDLERAFSRF GDILDCQIML ERDTGRSRGF GFITFADRRA
MDESIREMHG RDFGDRVISV NRAEPKLGRD DGESHGSRGG RDSGYSIAGK GSFGGGGGGG
GRVGEDECFK CGRVGHWARD CPSAGGGRGG PVGGFSSRAS AYGGSDGRVD RYADRDRYVD
RERYIDDRYD GAARYGARDR FDSREAYIPR DRYASDRYAA PADRFAGGDR YSRGSDRYPP
GSYDKARSFE RDIAPSAGSD RYGGGRAGGP IRGGGEEGRG FRSRAGAPYE RPSRSGGGGA
YPSSSTFDRY
